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果蝇Ca2+/钙调蛋白依赖性一氧化氮合酶dNOS的分子与生化特性

Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase.

作者信息

Regulski M, Tully T

机构信息

Cold Spring Harbor Laboratory, NY 11724, USA.

出版信息

Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9072-6. doi: 10.1073/pnas.92.20.9072.

DOI:10.1073/pnas.92.20.9072
PMID:7568075
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC40926/
Abstract

Nitric oxide (NO) is an intercellular messenger involved with various aspects of mammalian physiology ranging from vasodilation and macrophage cytotoxicity to neuronal transmission. NO is synthesized from L-arginine by NO synthase (NOS). Here, we report the cloning of a Drosophila NOS gene, dNOS, located at cytological position 32B. The dNOS cDNA encodes a protein of 152 kDa, with 43% amino acid sequence identity to rat neuronal NOS. Like mammalian NOSs, DNOS protein contains putative binding sites for calmodulin, FMN, FAD, and NADPH. DNOS activity is Ca2+/calmodulin dependent when expressed in cell culture. An alternative RNA splicing pattern also exists for dNOS, which is identical to that for vertebrate neuronal NOS. These structural and functional observations demonstrate remarkable conservation of NOS between vertebrates and invertebrates.

摘要

一氧化氮(NO)是一种细胞间信使,参与哺乳动物生理学的各个方面,从血管舒张、巨噬细胞细胞毒性到神经传递。NO由一氧化氮合酶(NOS)从L-精氨酸合成。在此,我们报告了一个位于细胞学位置32B的果蝇NOS基因dNOS的克隆。dNOS cDNA编码一种152 kDa的蛋白质,与大鼠神经元NOS的氨基酸序列同一性为43%。与哺乳动物的NOS一样,DNOS蛋白含有钙调蛋白、FMN、FAD和NADPH的假定结合位点。当在细胞培养中表达时,DNOS活性依赖于Ca2+/钙调蛋白。dNOS也存在一种替代的RNA剪接模式,这与脊椎动物神经元NOS的模式相同。这些结构和功能观察结果表明,脊椎动物和无脊椎动物的NOS具有显著的保守性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f61/40926/e367eb287222/pnas01498-0073-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f61/40926/e17766702b15/pnas01498-0072-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f61/40926/e367eb287222/pnas01498-0073-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f61/40926/e17766702b15/pnas01498-0072-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3f61/40926/e367eb287222/pnas01498-0073-a.jpg

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